Đang chuẩn bị liên kết để tải về tài liệu:
Báo cáo khoa học: Physiological relevance of the endogenous mono(ADP-ribosyl)ation of cellular proteins

The mono(ADP-ribosyl)ation reaction is a post-translational modification that is catalysed by both bacterial toxins and eukaryotic enzymes, and that results in the transfer of ADP-ribose from bNAD + to various acceptor proteins. In mammals, both intracellular and extracellular reactions have been described; the latter are due to glycosylphosphatidylinositol-anchored or secreted enzymes that are able to modify their targets, which include the purinergic receptor P2X7, the defensins and the integrins. . | ềFEBS Journal MINIREVIEW Physiological relevance of the endogenous mono ADP-ribosyl ation of cellular proteins Maria Di Girolamo Nadia Dani Annalisa Stilla and Daniela Corda Department of Cell Biology and Oncology Consorzio Mario Negri Sud Santa Maria Imbaro Chieti Italy Keywords mono ADP-ribosyl ation ADP-ribosyltransferase ART G-protein defensin apoptosis P2X7 Correspondence D. Corda or M. Di Girolamo Consorzio Mario Negri Sud Department of Cell Biology and Oncology 66030 Santa Maria Imbaro Chieti Italy Fax 39 0872 570 412 Tel 39 0872 570 338 E-mail corda@negrisud.it mdigirolamo@negrisud.it Website http www.negrisud.it en dcbo The mono ADP-ribosyl ation reaction is a post-translational modification that is catalysed by both bacterial toxins and eukaryotic enzymes and that results in the transfer of ADP-ribose from PNAD to various acceptor proteins. In mammals both intracellular and extracellular reactions have been described the latter are due to glycosylphosphatidylinositol-anchored or secreted enzymes that are able to modify their targets which include the purinergic receptor P2X7 the defensins and the integrins. Intracellular mono ADP-ribosyl ation modifies proteins that have roles in cell signalling and metabolism such as the chaperone GRP78 BÍP the b-subunit of heterotrimeric G-proteins and glutamate dehydrogenase. The molecular identification of the intracellular enzymes however is still missing. A better molecular understanding of this reaction will help in the full definition of its role in cell physiology and pathology. Received 18 April 2005 accepted 18 July 2005 doi 10.1111 j.1742-4658.2005.04876.x Enzyme-modulated mono ADP-ribosyl ation was originally identified as the mechanism of action of several of the bacterial toxins 1 . The diphtheria cholera pertussis and clostridia toxins are mono ADP-ribo-syl transferases ARTs EC 2.4.2.31 and they are known to cause various pathologies after their translocation into mammalian host cells. Once inside the cell